Kelsi R. Hall

Introduction Click to copy section linkSection link copied! The catalytic capabilities of lytic polysaccharide monooxygenases (LPMOs) were first discovered in 2010 (1) and LPMOs have since garnered significant attention due to their unique catalytic power and biotechnological applications.

Abstract Oxidoreductases have evolved tyrosine/tryptophan pathways that channel highly oxidizing holes away from the active site to avoid damage. Here we dissect such a pathway in a bacterial LPMO, member of a widespread family of C-H bond activating enzymes with outstanding industrial potential. We show that a strictly conserved tryptophan is critical for radical formation and hole transference and that holes traverse the protein to reach a tyrosine-histidine pair in the protein’s surface.

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